Murphy C L, Eulitz M, Hrncic R, Sletten K, Westermark P, Williams T, Macy S D, Wooliver C, Wall J, Weiss D T, Solomon A
University of Tennessee Graduate School of Medicine, Knoxville, TN, USA.
Am J Clin Pathol. 2001 Jul;116(1):135-42. doi: 10.1309/TWBM-8L4E-VK22-FRH5.
The human amyloidoses represent a heterogeneous group of disorders characterized by the deposition of fibrillar protein in vital organs. Given the fact that at least 20 different molecules can form fibrils, the unambiguous identification of the type of amyloid deposited is critical to the correct diagnosis and treatment of patients with these disorders. Heretofore, this information has been inferred from particular clinical features of the disease, ancillary laboratory tests, and results of immunohistochemical analyses. However, to establish unequivocally the kind of protein that is deposited as amyloid, it is necessary to determine its chemical composition through amino acid sequencing or mass spectroscopy of material extracted from fibrillar deposits. We have developed a micromethod whereby such studies can be performed readily using sections of formalin-fixed, paraffin-embedded biopsy specimens. The ability to identify precisely the nature of the tissue deposits has diagnostic, therapeutic, and prognostic implications for patients with amyloid-associated disorders.
人类淀粉样变性是一组异质性疾病，其特征是在重要器官中沉积纤维状蛋白质。鉴于至少有20种不同的分子可形成纤维，明确所沉积淀粉样蛋白的类型对于这些疾病患者的正确诊断和治疗至关重要。迄今为止，这些信息是从疾病的特定临床特征、辅助实验室检查以及免疫组织化学分析结果中推断出来的。然而，要明确确定作为淀粉样蛋白沉积的蛋白质种类，有必要通过对从纤维状沉积物中提取的物质进行氨基酸测序或质谱分析来确定其化学组成。我们已经开发出一种微量方法，通过该方法可以使用福尔马林固定、石蜡包埋活检标本的切片轻松进行此类研究。精确识别组织沉积物性质的能力对淀粉样变性相关疾病患者具有诊断、治疗和预后意义。
